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1kql

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kql OCA], [http://www.ebi.ac.uk/pdbsum/1kql PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kql RCSB]</span>
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[[Category: tropomyosin]]
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Revision as of 18:52, 30 March 2008


PDB ID 1kql

Drag the structure with the mouse to rotate
, resolution 2.70Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the C-terminal region of striated muscle alpha-tropomyosin at 2.7 angstrom resolution


Overview

Contraction in striated and cardiac muscles is regulated by the motions of a Ca(2+)-sensitive tropomyosin/troponin switch. In contrast, troponin is absent in other muscle types and in nonmuscle cells, and actomyosin regulation is myosin-linked. Here we report an unusual crystal structure at 2.7 A of the C-terminal 31 residues of rat striated-muscle alpha-tropomyosin (preceded by a fragment of the GCN4 leucine zipper). The C-terminal 22 residues (263-284) of the structure do not form a two-stranded alpha-helical coiled coil as does the rest of the molecule, but here the alpha-helices splay apart and are stabilized by the formation of a tail-to-tail dimer with a symmetry-related molecule. The site of splaying involves a small group of destabilizing core residues that is present only in striated muscle tropomyosin isoforms. These results reveal a specific recognition site for troponin T and clarify the physical basis for the unique regulatory mechanism of striated muscles.

About this Structure

1KQL is a Single protein structure of sequence from Saccharomyces cerevisiae and rattus norvegicus. Full crystallographic information is available from OCA.

Reference

The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site., Li Y, Mui S, Brown JH, Strand J, Reshetnikova L, Tobacman LS, Cohen C, Proc Natl Acad Sci U S A. 2002 May 28;99(11):7378-83. PMID:12032291

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